1AST

STRUCTURE OF ASTACIN AND IMPLICATIONS FOR ACTIVATION OF ASTACINS AND ZINC-LIGATION OF COLLAGENASES

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004222	molecular_function	metalloendopeptidase activity
A	0006508	biological_process	proteolysis
A	0008237	molecular_function	metallopeptidase activity
A	0008270	molecular_function	zinc ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 999

Chain	Residue
A	HIS92
A	HIS96
A	HIS102
A	TYR149
A	HOH300

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site_id	CAT
Number of Residues	4
Details	CATALYTIC SITE

Chain	Residue
A	HIS92
A	HIS96
A	HIS102
A	TYR149

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Functional Information from PROSITE/UniProt

site_id	PS00142
Number of Residues	10
Details	ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TIIHELMHAI

Chain	Residue	Details
A	THR89-ILE98

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU01211, ECO:0000305|PubMed:1319561

Chain	Residue	Details
A	GLU93

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site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01211, ECO:0000269|PubMed:1319561, ECO:0000269|PubMed:8756323

Chain	Residue	Details
A	HIS92
A	HIS96
A	HIS102

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 20202938, 11078883, 7674922

Chain	Residue	Details
A	GLU93
A	TYR149

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site_id	MCSA1
Number of Residues	5
Details	M-CSA 403

Chain	Residue	Details
A	HIS92	metal ligand
A	GLU93	proton shuttle (general acid/base)
A	HIS96	metal ligand
A	HIS102	metal ligand
A	TYR149	transition state stabiliser

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